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- W2886782802 endingPage "2145" @default.
- W2886782802 startingPage "2136" @default.
- W2886782802 abstract "All proteins contain characteristic backbones formed of consecutive amide bonds, which can engage in hydrogen bonds. However, the importance of these is not easily addressed by conventional technologies that only allow for side-chain substitutions. By contrast, technologies such as nonsense suppression mutagenesis and protein ligation allow for manipulation of the protein backbone. In particular, replacing the backbone amide groups with ester groups, that is, amide-to-ester mutations, is a powerful tool to examine backbone-mediated hydrogen bonds. In this minireview, we showcase examples of how amide-to-ester mutations can be used to uncover pivotal roles of backbone-mediated hydrogen bonds in protein recognition, folding, function, and structure." @default.
- W2886782802 created "2018-08-22" @default.
- W2886782802 creator A5045259945 @default.
- W2886782802 creator A5045372915 @default.
- W2886782802 creator A5060992391 @default.
- W2886782802 creator A5062421025 @default.
- W2886782802 creator A5066198767 @default.
- W2886782802 creator A5072904379 @default.
- W2886782802 date "2018-10-01" @default.
- W2886782802 modified "2023-10-05" @default.
- W2886782802 title "Probing Backbone Hydrogen Bonds in Proteins by Amide-to-Ester Mutations" @default.
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